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1ck7
From Proteopedia
GELATINASE A (FULL-LENGTH)
Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed., Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K, Science. 1999 Jun 4;284(5420):1667-70. PMID:10356396
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1CK7 is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K. Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. Science. 1999 Jun 4;284(5420):1667-70. PMID:10356396
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